A new time-resolved fluorescence spectrophotometer was developed to provide rapid collection and analysis of macromolecular size, decay lifetimes, and spectra. The instrument was exploited to study protein associations (eg; conformational changes in OTCase and arginase with P. Hensley, Georgetown; enzyme I dimerization with M Han, L. Brand, S. Roseman, JHU; decays of glutamine synthetase with A. Ginsburg, H/LB; eu.if.2 with D. Goss, CUNY). The system was modified to speed reduction/oxidation and folding, with M. Han, C. Anfinsen, L. Brand, JHU; rapid denaturation of HLADH monitored by lifetime and rotation changes. Model tryptophyl-related systems (melatonin, serotonin, trp peptides, copper and nickel quenchings ) were examine with Dr. Chen. "Global analysis" methods were developed to quantitate macromolecule axial ratios, to study proteins and lipids exhibiting distributed decay, and to link spectral signatures to conformations. A variety of other biochemical applications - Aggregation and self quenching of solutes inside liposomes (R. Chen H:LTD). Sulfhydryl probes for oxidation defense profiles (A Russo C:ROB). Tryptophyl fluorescence changes accompany oxidation damage of enzymes (B. Taffe JHU, R. Levine H:LB). DNA carcinogen adduct detection (D. Manchester C:LMC), Microwave effects on liposome structure (C Rafferty WRAIR). Structural fluctuations in lipid bilayers (L. Davenport CUNY). Several other new laser fluorescence instruments were designed and are being prototyped continuously.